5gi4: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/DEAD_ECOLI DEAD_ECOLI] DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity at low temperature. Involved in 50S ribosomal subunit assembly, acting after SrmB, and could also play a role in the biogenesis of the 30S ribosomal subunit. In addition, is involved in mRNA decay, via formation of a cold-shock degradosome with RNase E. Also stimulates translation of some mRNAs, probably at the level of initiation.[HAMAP-Rule:MF_00964]<ref>PMID:10216955</ref> <ref>PMID:15148362</ref> <ref>PMID:15196029</ref> <ref>PMID:15554978</ref> <ref>PMID:17259309</ref> <ref>PMID:8552679</ref>  
[https://www.uniprot.org/uniprot/DEAD_ECOLI DEAD_ECOLI] DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity at low temperature. Involved in 50S ribosomal subunit assembly, acting after SrmB, and could also play a role in the biogenesis of the 30S ribosomal subunit. In addition, is involved in mRNA decay, via formation of a cold-shock degradosome with RNase E. Also stimulates translation of some mRNAs, probably at the level of initiation.[HAMAP-Rule:MF_00964]<ref>PMID:10216955</ref> <ref>PMID:15148362</ref> <ref>PMID:15196029</ref> <ref>PMID:15554978</ref> <ref>PMID:17259309</ref> <ref>PMID:8552679</ref>  
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== Publication Abstract from PubMed ==
CsdA has been proposed to be essential for the biogenesis of ribosome and gene regulation after cold shock. However, the structure of CsdA and the function of its long C-terminal regions are still unclear. Here, we solved all of the domain structures of CsdA and found two previously uncharacterized auxiliary domains: a dimerization domain (DD) and an RNA-binding domain (RBD). Small-angle X-ray scattering experiments helped to track the conformational flexibilities of the helicase core domains and C-terminal regions. Biochemical assays revealed that DD is indispensable for stabilizing the CsdA dimeric structure. We also demonstrate for the first time that CsdA functions as a stable dimer at low temperature. The C-terminal regions are critical for RNA binding and efficient enzymatic activities. CsdA_RBD could specifically bind to the regions with a preference for single-stranded G-rich RNA, which may help to bring the helicase core to unwind the adjacent duplex.
Insights into the Structure of Dimeric RNA Helicase CsdA and Indispensable Role of Its C-Terminal Regions.,Xu L, Wang L, Peng J, Li F, Wu L, Zhang B, Lv M, Zhang J, Gong Q, Zhang R, Zuo X, Zhang Z, Wu J, Tang Y, Shi Y Structure. 2017 Dec 5;25(12):1795-1808.e5. doi: 10.1016/j.str.2017.09.013. Epub, 2017 Oct 26. PMID:29107486<ref>PMID:29107486</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==

Latest revision as of 12:12, 20 March 2024

DEAD-box RNA helicaseDEAD-box RNA helicase

Structural highlights

5gi4 is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.244Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DEAD_ECOLI DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity at low temperature. Involved in 50S ribosomal subunit assembly, acting after SrmB, and could also play a role in the biogenesis of the 30S ribosomal subunit. In addition, is involved in mRNA decay, via formation of a cold-shock degradosome with RNase E. Also stimulates translation of some mRNAs, probably at the level of initiation.[HAMAP-Rule:MF_00964][1] [2] [3] [4] [5] [6]

See Also

References

  1. ↑ Lu J, Aoki H, Ganoza MC. Molecular characterization of a prokaryotic translation factor homologous to the eukaryotic initiation factor eIF4A. Int J Biochem Cell Biol. 1999 Jan;31(1):215-29. PMID:10216955
  2. ↑ Charollais J, Dreyfus M, Iost I. CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in the biogenesis of 50S ribosomal subunit. Nucleic Acids Res. 2004 May 17;32(9):2751-9. Print 2004. PMID:15148362 doi:10.1093/nar/gkh603
  3. ↑ Bizebard T, Ferlenghi I, Iost I, Dreyfus M. Studies on three E. coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases. Biochemistry. 2004 Jun 22;43(24):7857-66. PMID:15196029 doi:10.1021/bi049852s
  4. ↑ Prud'homme-Genereux A, Beran RK, Iost I, Ramey CS, Mackie GA, Simons RW. Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome'. Mol Microbiol. 2004 Dec;54(5):1409-21. PMID:15554978 doi:http://dx.doi.org/10.1111/j.1365-2958.2004.04360.x
  5. ↑ Turner AM, Love CF, Alexander RW, Jones PG. Mutational analysis of the Escherichia coli DEAD box protein CsdA. J Bacteriol. 2007 Apr;189(7):2769-76. Epub 2007 Jan 26. PMID:17259309 doi:http://dx.doi.org/10.1128/JB.01509-06
  6. ↑ Jones PG, Mitta M, Kim Y, Jiang W, Inouye M. Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli. Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):76-80. PMID:8552679

5gi4, resolution 2.24Å

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